ID   GPX1_SAPAP              Reviewed;         201 AA.
AC   Q4AEI1;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Glutathione peroxidase 1 {ECO:0000305};
DE            Short=GPx-1;
DE            Short=GSHPx-1;
DE            EC=1.11.1.9 {ECO:0000250|UniProtKB:P07203};
DE   AltName: Full=Cellular glutathione peroxidase;
GN   Name=GPX1;
OS   Sapajus apella (Brown-capped capuchin) (Cebus apella).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Cebinae; Sapajus.
OX   NCBI_TaxID=9515;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15967696; DOI=10.1016/j.cbpc.2005.05.002;
RA   Fukuhara R., Kageyama T.;
RT   "Structure, gene expression, and evolution of primate glutathione
RT   peroxidases.";
RL   Comp. Biochem. Physiol. 141B:428-436(2005).
CC   -!- FUNCTION: Protects the hemoglobin in erythrocytes from oxidative
CC       breakdown. In platelets, plays a crucial role of glutathione peroxidase
CC       in the arachidonic acid metabolism. {ECO:0000250|UniProtKB:P11352}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O;
CC         Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
CC         Evidence={ECO:0000250|UniProtKB:P11352};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834;
CC         Evidence={ECO:0000250|UniProtKB:P11352};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2
CC         glutathione = (12S)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate +
CC         glutathione disulfide + H2O; Xref=Rhea:RHEA:50708, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57444, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297,
CC         ChEBI:CHEBI:90680; Evidence={ECO:0000250|UniProtKB:P11352};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50709;
CC         Evidence={ECO:0000250|UniProtKB:P11352};
CC   -!- SUBUNIT: Homotetramer. Interacts with MIEN1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: During periods of oxidative stress, Sec-47 may react with a
CC       superoxide radical, irreversibly lose hydroselenide and be converted to
CC       dehydroalanine. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB120999; BAE17009.1; -; mRNA.
DR   PeroxiBase; 3638; CapGPx01.
DR   Proteomes; UP000504640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004602; F:glutathione peroxidase activity; ISS:UniProtKB.
DR   GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; ISS:UniProtKB.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0019372; P:lipoxygenase pathway; ISS:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd00340; GSH_Peroxidase; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR029759; GPX_AS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11592; PTHR11592; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Lipid metabolism; Oxidoreductase; Peroxidase;
KW   Phosphoprotein; Reference proteome; Selenocysteine.
FT   CHAIN           1..201
FT                   /note="Glutathione peroxidase 1"
FT                   /id="PRO_0000066609"
FT   ACT_SITE        47
FT                   /evidence="ECO:0000250"
FT   SITE            47
FT                   /note="Subject to oxidation and hydroselenide loss to
FT                   dehydroalanine"
FT                   /evidence="ECO:0000250"
FT   NON_STD         47
FT                   /note="Selenocysteine"
FT   MOD_RES         32
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04041"
FT   MOD_RES         86
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P11352"
FT   MOD_RES         86
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P11352"
FT   MOD_RES         112
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P11352"
FT   MOD_RES         112
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P11352"
FT   MOD_RES         146
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P11352"
FT   MOD_RES         146
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P11352"
FT   MOD_RES         195
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04041"
FT   MOD_RES         199
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P07203"
SQ   SEQUENCE   201 AA;  21785 MW;  E976C3CF4782BBD8 CRC64;
     MCAAGLAAAA AQSVYAFSAR QLAGGEPVSL GSLRCKGLLI ENVASLUGTT VRDYTQMNEP
     QRRLGPRGLV VLGFPCNHSG HQENAKNEEI LNSLKYVRPG GGFEPNFMLF EKGEVNGAGA
     HTLFAFLREA LPAPSDDATA LMIDPKLITW SPVCRNDVAW NFEKFLVGPD GVPLRRYSRR
     FQTIDIEPDI EALLSQGPSC A